Adsorption behavior and stabilization/destabilization effects of 2-hydroxyethyl methacrylate(HEMA)on a bovine tendon collagen(BTC) (type I) , either native(N)or thermally denatured(D) , were studied by IR spectroscopy and differential scanning calorimetry(DSC) . The amount of HEMA adsorbed was larger on BTC (D)than on BTC (N) , because BTC (D)had a larger specific surface area(SSA)as revealed from SSA measurement. Denaturation temperature(T d )of BTC (N) , measured by DSC in aqueous HEMA solution, decreased from 63℃ to 40℃ with increasing HEMA concentration(C HEMA )up to 20 wt%. This destabilization might be caused by the loss of hydrophobic stabilization of the helix structure as C HEMA was increased. At C HEMA >20 wt%, the structure of collagen was restabilized presumably due to the dehydration effect conferred by HEMA at higher concentration. BTC (D)with little helix content, however, showed only a weak endothermic peak in the DSC measurement and the T d at 40℃ was independent of C HEMA .
Effects of hydrophobic environment adjusted by various alcohols on the structural stability of calfskin collagen (CSC) were studied to elucidate the nature of collagen-monomer interaction in adhesion. The stability of CSC in aqueous alcohol solutions was represented by its denaturation temperature, Td, measured by DSC. The hydrophobicity of the alcohol solutions was quantified with their specific dielectric constants, εr, calculated from their concentrations. The effect of each alcohol to stabilize or destabilize CSC was evaluated by the initial slope of each Td vs. εr plot, denoted as -(dTd/dεr)ini and termed as stabilization power. Results showed that a hydrophobic environment with a smaller εr lowered the stabilization power. Stabilization power ranged from -3 (strong destabilization) for phenol (εr=12) to +0.3 (weak stabilization) for glycerol (εr=47). In view of the encouraging results obtained in this study, the new index was therefore helpful in predicting the effects of new dental materials of known εr values on the stability of dentinal collagen.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.